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Biochem Biophys Res Commun. 1988 Dec 30;157(3):937-43.

Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous.

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Howard Hughes Medical Institute, Department of Biochemistry, University of Chicago, IL 60637.


cDNA clones encoding human hexokinase have been isolated from an adult kidney library. Analysis of this 917 amino acid protein (Mr = 102,519) indicates that the sequences of the NH2- and COOH-terminal halves, corresponding to the regulatory and catalytic domains, respectively, are homologous; and that eukaryotic hexokinases evolved by duplication of a gene encoding a protein of 450 amino acids. The COOH-terminal half of the protein created by this gene duplication retained the glucose binding site and glucose phosphorylating activity while the substrate binding sites of the NH2-terminal half evolved into a new allosteric effector site.

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